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Metabolic Engineering for the Production of a Variety of Biofuels and Biochemicals
Published in Kazuyuki Shimizu, Metabolic Regulation and Metabolic Engineering for Biofuel and Biochemical Production, 2017
On the other hand, the over-expression of the respiratory pathway for glycerol uptake causes the decrease in ethanol production, while significantly increases D-lactate production (Mazumdar et al. 2010). This pathway involves a respiratory GLPDH that donates electrons directly to quinol/quinone (Schweizer and Larson 1987, Walz et al. 2002), where the electrons are then transferred to oxygen via cytochrome oxidases under aerobic condition. Under micro-aerobic or anaerobic conditions, NADH produced at GAPDH is balanced with the consumption at LDH with the ATP production at Pyk by the substrate level phosphorylation.
Interfacial Catalysis at Oil/Water Interfaces
Published in Alexander G. Vdlkdv, Interfacial Catalysis, 2002
Dependence of the catalytic activity (maximal rate) of (a) glyceraldehyde-3-phosphate dehydrogenase, GAPDH; (b) lactate dehydrogenase, LDH; and (c) their heteroenzyme complexes, GAPDH + LDH, on the degree of surfactant (water-to-AOT molar ratio) in reverse micelles of AOT in octane. (From Ref. 60. )
Allergenicity assessment of fungal species using immunoclinical and proteomic techniques: a study on Fusarium lateritium
Published in International Journal of Environmental Health Research, 2020
Debarati Dey, Swati Gupta Bhattacharya
Identification of allergens from environmental fungi is beneficial in the diagnosis and treatment of clinical fungal allergy. Glyceraldehyde-3-phosphate dehydrogenase was found to be present in 81.81% of F. lateritium sensitized patients and no other 34 kDa protein was found in 2D immunoblots. This made the 34 kDa Glyceraldehyde-3-phosphate dehydrogenase protein a potential allergen of F. lateritium. This protein is an enzyme of ~37 kDa that catalyzes the sixth step of glycolysis and thus serves to break down glucose for energy and carbon molecules. In addition to this long-established metabolic function, GAPDH has recently been implicated in several non-metabolic processes, including transcription activation, initiation of apoptosis (Nicholls et al. 2012), ER to Golgi vesicle shuttling, and fast axonal, or axoplasmic transport (Tristan et al. 2011). Purification and characterization of this particular protein may improve component-resolved diagnosis and therapy of F. lateritium sensitized patients.
Chronic exposure to environmentally relevant levels of simvastatin disrupts zebrafish brain gene signaling involved in energy metabolism
Published in Journal of Toxicology and Environmental Health, Part A, 2020
Susana Barros, Ana M. Coimbra, Nélson Alves, Marlene Pinheiro, José Benito Quintana, Miguel M. Santos, Teresa Neuparth
Similar to mammals, fish brain relies mostly on glucose metabolism for the production of acetyl-CoA, essential for the tricarboxylic acid cycle. Nowis et al. (2014) reported that in cultured human muscle cells SIM, as well as other statins, were able to alter gene transcription of glut1b limiting glucose transport to the brain. Our results showed that transcription of glut1b was altered at the intermediate SIM concentrations, 40 ng/L and/or 200 ng/L (a downregulation in males and an upregulation in females) which suggests that glucose uptake may be altered in brain cells. These findings are supported by the noted alterations in gapdh mRNA levels. gapdh is known to be a multifunctional protein, involved in several biological processes, essential for glucose metabolism by its implication in glycolysis and glycogenesis (Figure 1) (Kadmiri et al. 2014; Zala et al. 2013). When glucose is reduced, brain cells also rely on fatty acid β-oxidation to obtain energy through the acetyl-CoA that participates in the TCA cycle (Lyssimachou et al. 2015; Soengas and Aldegunde 2002)(Figure 1). Data demonstrated that acadm, involved in the fatty acid β-oxidation, exhibited altered transcription levels, indicating a potential modulation of glucose metabolism.